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Mycolicibacterium smegmatis possesses operational agmatinase but contains no detectable polyamines
Mikhail Zamakhaev1, Ivan Tsyganov2, Larisa Nesterova2
1Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, Moscow, Russia.
Background:
Polyamines are widespread intracellular molecules able to influence antibiotic susceptibility, but almost nothing is known on their occurrence and physiological role in mycobacteria.
Methods:
here, we analyzed transcriptomic, proteomic and biochemical data and obtained the first evidence for the post-transcriptional expression of some genes attributed to polyamine metabolism and polyamine transport in Mycolicibacterium smegmatis (basionym Mycobacterium smegmatis).
Results:
in our experiments, exponentially growing cells demonstrated transcription of 21 polyamine-associated genes and possessed 7 enzymes of polyamine metabolism and 2 polyamine transport proteins.
Conclusion:
Mycolicibacterium smegmatis putrescine synthesizing enzyme agmatinase SpeB was originally shown to catalyze agmatine conversion to putrescine in vitro. Nevertheless, we have not found any polyamines in mycobacterial cells.
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